+
Open data
-
Basic information
Entry | Database: PDB / ID: 1dsj | ||||||
---|---|---|---|---|---|---|---|
Title | NMR SOLUTION STRUCTURE OF VPR50_75, 20 STRUCTURES | ||||||
![]() | VPR PROTEIN | ||||||
![]() | VIRAL PEPTIDE / POLYPEPTIDE | ||||||
Function / homology | ![]() symbiont-mediated arrest of host cell cycle during G2/M transition / monoatomic ion transmembrane transport / host cell / virion component / protein homooligomerization / viral penetration into host nucleus / host extracellular space / symbiont entry into host cell / cell cycle / DNA-templated transcription ...symbiont-mediated arrest of host cell cycle during G2/M transition / monoatomic ion transmembrane transport / host cell / virion component / protein homooligomerization / viral penetration into host nucleus / host extracellular space / symbiont entry into host cell / cell cycle / DNA-templated transcription / host cell nucleus / regulation of DNA-templated transcription Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Yao, S. / Torres, A.M. / Azad, A.A. / Macreadie, I.G. / Norton, R.S. | ||||||
![]() | Journal: Protein Pept.Lett. / Year: 1998 Title: Helical structure of polypeptides from the C-terminal half of HIV-1 VPR. Authors: Yao, S.G. / Azad, A.A. / Macreadie, I.G. / Norton, R.S. #1: ![]() Title: Vpr Protein of Human Immunodeficiency Virus Type 1 Forms Cation-Selective Channels in Planar Lipid Bilayers Authors: Piller, S.C. / Ewart, G.D. / Premkumar, A. / Cox, G.B. / Gage, P.W. #2: ![]() Title: A Domain of Human Immunodeficiency Virus Type 1 Vpr Containing Repeated H(S/F)Rig Amino Acid Motifs Causes Cell Growth Arrest and Structural Defects Authors: Macreadie, I.G. / Castelli, L.A. / Hewish, D.R. / Kirkpatrick, A. / Ward, A.C. / Azad, A.A. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 176.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 152.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 350.5 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 440.5 KB | Display | |
Data in XML | ![]() | 9.9 KB | Display | |
Data in CIF | ![]() | 16.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | Mass: 3057.594 Da / Num. of mol.: 1 / Fragment: RESIDUES 50 - 75 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|
-
Sample preparation
Sample conditions | pH: 3.3 / Temperature: 298 K |
---|---|
Crystal grow | *PLUS Method: other / Details: NMR |
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 20 |